Academic Journal
Isolation and characterization of plant plasma membrane P-type H+-ATPase dimers.
| Τίτλος: | Isolation and characterization of plant plasma membrane P-type H+-ATPase dimers. |
|---|---|
| Συγγραφείς: | Malysenko E; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany., Günther Pomorski T; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany.; Department of Plant and Environmental Sciences, University of Copenhagen, 1871, Frederiksberg, Denmark., Justesen BH; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany. bo.justesen@ruhr-uni-bochum.de. |
| Πηγή: | Scientific reports [Sci Rep] 2026 Sep 15; Vol. 16 (1). Date of Electronic Publication: 2026 Sep 15. |
| Τύπος έκδοσης: | Journal Article; Research Support, Non-U.S. Gov't |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: London : Nature Publishing Group, copyright 2011- |
| Ιατρικοί όροι (MeSH): | Proton-Translocating ATPases*/chemistry , Proton-Translocating ATPases*/isolation & purification , Proton-Translocating ATPases*/metabolism , Cell Membrane*/enzymology , Arabidopsis Proteins*/chemistry , Arabidopsis Proteins*/metabolism , Arabidopsis Proteins*/isolation & purification , Arabidopsis*/enzymology , Protein Multimerization*, Liposomes/metabolism ; Chromatography, Gel |
| Περίληψη: | Plant H⁺-ATPases are activated through tightly regulated hexameric assembly, relieving autoinhibition via displacement of a regulatory domain during the oligomerization process. Sub-hexameric assembly states also exist but their role in activity regulation remains elusive. To characterize sub-hexameric plant H⁺-ATPases, we isolated homo-oligomers of the H⁺-ATPases AHA2 and determined their sizes with size exclusion chromatography multi-angle light scattering. AHA2 predominantly presented as a monomer but also assembled into stable dimers and larger complexes. Activity assays on solubilized and liposome-reconstituted AHA2 monomers and dimers revealed that dimerization did not affect enzymatic activity, suggesting that AHA2 dimerization does not represent a separate regulatory pathway. Instead, AHA2 dimers may serve as reservoirs for rapid hexamer assembly, facilitating the dynamic regulation of protein activity. (© 2026. The Author(s).) |
| Competing Interests: | Declarations. Competing interests: The authors declare no competing interests. |
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| Contributed Indexing: | Keywords: Dimers; H+-ATPase; Membrane reconstitution; Oligomers; Proton pumping; SEC-MALS |
| Substance Nomenclature: | EC 3.6.3.14 (Proton-Translocating ATPases) 0 (Arabidopsis Proteins) 0 (Liposomes) EC 7.1.2.1 (AHA2 protein, Arabidopsis) |
| Entry Date(s): | Date Created: 20260916 Date Completed: 20260916 Latest Revision: 20260918 |
| Update Code: | 20260918 |
| PubMed Central ID: | PMC13578685 |
| DOI: | 10.1038/s41598-026-70970-z |
| PMID: | 42744987 |
| Βάση Δεδομένων: | MEDLINE |
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